MARCKS
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesMARCKS, 80K-L, MACS, PKCSL, PRKCSL, myristoylated alanine rich protein kinase C substrate
External IDsOMIM: 177061 HomoloGene: 135584 GeneCards: MARCKS
Orthologs
SpeciesHumanMouse
Entrez

4082

n/a

Ensembl

ENSG00000277443

n/a

UniProt

P29966

n/a

RefSeq (mRNA)

NM_002356

n/a

RefSeq (protein)

NP_002347

n/a

Location (UCSC)Chr 6: 113.86 – 113.86 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

Myristoylated alanine-rich C-kinase substrate is a protein that in humans is encoded by the MARCKS gene.[3][4][5] It plays important roles in cell shape, cell motility, secretion, transmembrane transport, regulation of the cell cycle, and neural development.[6] Recently, MARCKS has been implicated in the exocytosis of a number of vesicles and granules such as mucin and chromaffin. It is also the name of a protein family, of which MARCKS is the most studied member. They are intrinsically disordered proteins, with an acidic pH, with high proportions of alanine, glycine, proline, and glutamic acid. They are membrane-bound through a lipid anchor at the N-terminus, and a polybasic domain in the middle. They are regulated by Ca2+/calmodulin and protein kinase C. In their unphosphorylated form, they bind to actin filaments, causing them to crosslink, and sequester acidic membrane phospholipids such as PIP2.

The protein encoded by this gene is a substrate for protein kinase C. It is localized to the plasma membrane and is an actin filament crosslinking protein. Phosphorylation by protein kinase C or binding to calcium-calmodulin inhibits its association with actin and with the plasma membrane, leading to its presence in the cytoplasm. The protein is thought to be involved in cell motility, phagocytosis, membrane trafficking and mitogenesis.[5]

Interactions

MARCKS has been shown to interact with TOB1[7] and with NMT2.[8]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000277443 - Ensembl, May 2017
  2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. Hartwig JH, Thelen M, Rosen A, Janmey PA, Nairn AC, Aderem A (April 1992). "MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin". Nature. 356 (6370): 618–22. Bibcode:1992Natur.356..618H. doi:10.1038/356618a0. PMID 1560845. S2CID 4252140.
  4. Blackshear PJ (January 1993). "The MARCKS family of cellular protein kinase C substrates". The Journal of Biological Chemistry. 268 (3): 1501–4. doi:10.1016/S0021-9258(18)53878-3. PMID 8420923.
  5. 1 2 "Entrez Gene: MARCKS myristoylated alanine-rich protein kinase C substrate".
  6. Prieto D, Zolessi FR (January 2017). "Functional Diversification of the Four MARCKS Family Members in Zebrafish Neural Development". Journal of Experimental Zoology Part B: Molecular and Developmental Evolution. 328 (1–2): 119–138. Bibcode:2017JEZB..328..119P. doi:10.1002/jez.b.22691. PMID 27554589. S2CID 13263249.
  7. Jin Cho S, La M, Ahn JK, Meadows GG, Joe CO (May 2001). "Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation". Biochemical and Biophysical Research Communications. 283 (2): 273–7. doi:10.1006/bbrc.2001.4773. PMID 11327693.
  8. Selvakumar P, Lakshmikuttyamma A, Sharma RK (2009). "Biochemical characterization of bovine brain myristoyl-CoA:protein N-myristoyltransferase type 2". Journal of Biomedicine & Biotechnology. 2009: 907614. doi:10.1155/2009/907614. PMC 2737134. PMID 19746168.

Further reading

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